Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Levodione reductase

Gene

lvr

Organism
Leifsonia aquatica (Corynebacterium aquaticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the regio- and stereoselective reversible NAD-dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol).

Catalytic activityi

(4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone + NAD+ = (6R)-2,2,6-trimethyl-1,4-cyclohexanedione + NADH.

Enzyme regulationi

Strongly activated by monovalent cations, such as K+, Na+, and NH4+.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei103Role in the determination of stereospecificity1
Binding sitei152Substrate1
Active sitei165Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 42NAD1 PublicationAdd BLAST26

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Levodione reductase (EC:1.1.1.-)
Alternative name(s):
(6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase
Gene namesi
Name:lvr
OrganismiLeifsonia aquatica (Corynebacterium aquaticum)
Taxonomic identifieri144185 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrobacteriaceaeLeifsonia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103E → A, D, N or Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000547211 – 267Levodione reductaseAdd BLAST267

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 19Combined sources5
Turni20 – 22Combined sources3
Helixi24 – 35Combined sources12
Beta strandi39 – 45Combined sources7
Helixi47 – 60Combined sources14
Beta strandi66 – 70Combined sources5
Helixi76 – 90Combined sources15
Beta strandi94 – 98Combined sources5
Helixi109 – 111Combined sources3
Helixi114 – 124Combined sources11
Helixi126 – 142Combined sources17
Beta strandi146 – 150Combined sources5
Helixi153 – 155Combined sources3
Beta strandi160 – 162Combined sources3
Helixi163 – 183Combined sources21
Helixi184 – 186Combined sources3
Beta strandi189 – 195Combined sources7
Helixi201 – 210Combined sources10
Helixi215 – 223Combined sources9
Helixi234 – 244Combined sources11
Helixi247 – 249Combined sources3
Beta strandi256 – 260Combined sources5
Turni261 – 265Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IY8X-ray1.60A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ9LBG2.
SMRiQ9LBG2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LBG2.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9LBG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATSSPTTR FTDRVVLITG GGSGLGRATA VRLAAEGAKL SLVDVSSEGL
60 70 80 90 100
EASKAAVLET APDAEVLTTV ADVSDEAQVE AYVTATTERF GRIDGFFNNA
110 120 130 140 150
GIEGKQNPTE SFTAAEFDKV VSINLRGVFL GLEKVLKIMR EQGSGMVVNT
160 170 180 190 200
ASVGGIRGIG NQSGYAAAKH GVVGLTRNSA VEYGRYGIRI NAIAPGAIWT
210 220 230 240 250
PMVENSMKQL DPENPRKAAE EFIQVNPSKR YGEAPEIAAV VAFLLSDDAS
260
YVNATVVPID GGQSAAY
Length:267
Mass (Da):27,920
Last modified:October 1, 2000 - v1
Checksum:i6F05C89383500304
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042262 Genomic DNA. Translation: BAA95121.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042262 Genomic DNA. Translation: BAA95121.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IY8X-ray1.60A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ9LBG2.
SMRiQ9LBG2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LBG2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLVR_LEIAQ
AccessioniPrimary (citable) accession number: Q9LBG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.